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http://purl.uniprot.org/citations/21925384http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21925384http://www.w3.org/2000/01/rdf-schema#comment"The translation, localization, and degradation of cytoplasmic mRNAs are controlled by the formation and rearrangement of their mRNPs. The conserved Ded1/DDX3 DEAD-box protein functions in an unknown manner to affect both translation initiation and repression. We demonstrate that Ded1 first functions by directly interacting with eIF4G to assemble a Ded1-mRNA-eIF4F complex, which accumulates in stress granules. After ATP hydrolysis by Ded1, the mRNP exits stress granules and completes translation initiation. Thus, Ded1 functions both as a repressor of translation, by assembling an mRNP stalled in translation initiation, and as an ATP-dependent activator of translation, by resolving the stalled mRNP. These results identify Ded1 as a translation initiation factor that assembles and remodels an intermediate complex in translation initiation."xsd:string
http://purl.uniprot.org/citations/21925384http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2011.08.008"xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/author"Gao Z."xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/author"Parker R."xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/author"Jankowsky E."xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/author"Hilliker A."xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/pages"962-972"xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/title"The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex."xsd:string
http://purl.uniprot.org/citations/21925384http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/21925384http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21925384
http://purl.uniprot.org/citations/21925384http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21925384
http://purl.uniprot.org/uniprot/P06634#attribution-1170BDD74E31D1E97D7A552C65CCB191http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/P06634#attribution-95D71894B9F3A29AFDBA1067C11C3973http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/P39935#attribution-1170BDD74E31D1E97D7A552C65CCB191http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/#_A0A8H4BX52-mappedCitation-21925384http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/#_P39935-mappedCitation-21925384http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/#_P06634-mappedCitation-21925384http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/A0A8H4BX52http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/P06634http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21925384
http://purl.uniprot.org/uniprot/P39935http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21925384